Gel Properties and Structural Characteristics of Composite Gels of Soy Protein Isolate and Silver Carp Protein

Problems with silver carp protein (SCP) include a strong fishy odor, low gel strength of SCP surimi, and susceptibility to gel degradation. The objective of this study was to improve the gel quality of SCP. The effects of the addition of native soy protein isolate (SPI) and SPI subjected to papain-restricted hydrolysis on the gel characteristics and structural features of SCP were studied. The beta-sheet structures in SPI increased after papain treatment. SPI treated with papain was crosslinked with SCP using glutamine transaminase (TG) to form a composite gel. Compared with the control, the addition of modified SPI increased the hardness, springiness, chewiness, cohesiveness, and water-holding capacity (WHC) of the protein gel (p < 0.05). In particular, the effects were most significant when the degree of SPI hydrolysis (DH) was 0.5% (i.e., gel sample M-2). The molecular force results demonstrated that hydrogen bonding, disulfide bonding, and hydrophobic association are important molecular forces in gel formation. The addition of the modified SPI increases the number of hydrogen bonds and the disulfide bonds. Scanning electron microscopy (SEM) analysis showed that the papain modifications allowed the formation of a composite gel with a complex, continuous, and uniform gel structure. However, the control of the DH is important as additional enzymatic hydrolysis of SPI decreased TG crosslinking. Overall, modified SPI has the potential to improve SCP gel texture and WHC.

Automated summary

This study aimed to improve the gel quality of silver carp protein (SCP) by adding soy protein isolate (SPI) and using glutamine transaminase (TG) to form a composite gel. The addition of papain-treated SPI increased the hardness, springiness, chewiness, cohesiveness, and water-holding capacity (WHC) of the protein gel. Molecular force results showed that hydrogen bonding, disulfide bonding, and hydrophobic association played important roles in gel formation. Scanning electron microscopy (SEM) analysis revealed that the papain modifications allowed the formation of a complex, continuous, and uniform gel structure.